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Database: UniProt
Entry: A0A166MXM3_EXIGL
LinkDB: A0A166MXM3_EXIGL
Original site: A0A166MXM3_EXIGL 
ID   A0A166MXM3_EXIGL        Unreviewed;       363 AA.
AC   A0A166MXM3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-JUN-2023, entry version 20.
DE   SubName: Full=ATP-NAD kinase {ECO:0000313|EMBL:KZV78534.1};
DE   Flags: Fragment;
GN   ORFNames=EXIGLDRAFT_737475 {ECO:0000313|EMBL:KZV78534.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV78534.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV78534.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV78534.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the NAD kinase family.
CC       {ECO:0000256|ARBA:ARBA00010995}.
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DR   EMBL; KV426857; KZV78534.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166MXM3; -.
DR   STRING; 1314781.A0A166MXM3; -.
DR   InParanoid; A0A166MXM3; -.
DR   OrthoDB; 455155at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR   GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
DR   GO; GO:0006741; P:NADP biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   HAMAP; MF_00361; NAD_kinase; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_C.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR002504; NADK.
DR   PANTHER; PTHR20275; NAD KINASE; 1.
DR   PANTHER; PTHR20275:SF26; NADH KINASE POS5, MITOCHONDRIAL; 1.
DR   Pfam; PF01513; NAD_kinase; 1.
DR   Pfam; PF20143; NAD_kinase_C; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KZV78534.1};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          285..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          324..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         363
FT                   /evidence="ECO:0000313|EMBL:KZV78534.1"
SQ   SEQUENCE   363 AA;  39770 MW;  50D00F39E0F357B9 CRC64;
     MRAGPENILI VKKENDKRVR EAFHNIVGYM GRHHPKATLF HEDAPDIPPE LHKWRPSSGQ
     PIDLVITLGG DGTVLRVSSL FSTGPVPPVL SFSMGTLGFL LPFHIGSFET AIHHVFLGQA
     TVLPRMRLAC KFYDRDGLEF DGCGAGGWQV MNEVTLHRGR SPHLTTVDSY VDGQHLTEAV
     ADGLILSTPT GSTAYSLSSG GPIVHESVSA LLLTPICPRS LSFRPLLLPG SSRITLQLSE
     KSRAQSAEIF MDGKEARFLQ REEFVSIAAS RFPIPCVNRS SLGHFPVPTP TDDDSSPHHN
     HAPRAEDDWV RDINTLLQFN ATFRNKDQGL LRPPDPSEMD IPTAPKPKPE GGPSPGEHHR
     PPP
//
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